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Q27452 (PRP2_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenoloxidase subunit 2

EC=1.14.18.1
Alternative name(s):
PO 2
Tyrosinase 2
OrganismBombyx mori (Silk moth) [Reference proteome]
Taxonomic identifier7091 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Ref.1

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit By similarity. UniProtKB P04253

Subunit structure

Heterodimer. Ref.1

Subcellular location

Secreted.

Tissue specificity

Synthesized by hemocytes and released into the hemolymph plasma. Ref.1

Post-translational modification

The N-terminus is blocked. Ref.3

Sequence similarities

Belongs to the tyrosinase family.

Mass spectrometry

Molecular mass is 81105 Da from positions 52 - 693. Determined by MALDI. Ref.3

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5151 Ref.1
PRO_0000035901
Chain52 – 693642Phenoloxidase subunit 2 Ref.1
PRO_0000035902

Sites

Metal binding2131Copper A By similarity UniProtKB P04253
Metal binding2171Copper A By similarity UniProtKB P04253
Metal binding2431Copper A By similarity UniProtKB P04253
Metal binding3661Copper B By similarity UniProtKB P04253
Metal binding3701Copper B By similarity UniProtKB P04253
Metal binding4061Copper B By similarity UniProtKB P04253

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Potential
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Glycosylation4941N-linked (GlcNAc...) Potential
Glycosylation6801N-linked (GlcNAc...) Potential
Disulfide bond583 ↔ 627 By similarity
Disulfide bond585 ↔ 634 By similarity

Experimental info

Sequence conflict4331P → Q AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q27452 [UniParc].

Last modified January 1, 1999. Version 2.
Checksum: 013114DF4CC1A926

FASTA69380,119
        10         20         30         40         50         60 
MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI 

        70         80         90        100        110        120 
PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR 

       130        140        150        160        170        180 
VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR 

       190        200        210        220        230        240 
IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF 

       250        260        270        280        290        300 
YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD 

       310        320        330        340        350        360 
LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE 

       370        380        390        400        410        420 
LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA 

       430        440        450        460        470        480 
YVRPYTRSEL ENPGVQVRSV SVETPGGQPN TLNTFWMLSD VNLSRGLDFS DNGPVYARFT 

       490        500        510        520        530        540 
HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA 

       550        560        570        580        590        600 
GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG 

       610        620        630        640        650        660 
MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS 

       670        680        690 
LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV 

« Hide

References

[1]"Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin."
Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.
Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Kinshu X Showa.
Tissue: Hemocyte.
[2]Asano T., Ashida M.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori."
Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.
Arch. Biochem. Biophys. 320:14-23(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Hemocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49371 mRNA. Translation: BAA08369.1.
AB048762 mRNA. Translation: BAB41101.1.
RefSeqNP_001037534.1. NM_001044069.1.
UniGeneBmo.1389.

3D structure databases

ProteinModelPortalQ27452.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaBGIBMGA013115-RA; BGIBMGA013115-TA; BGIBMGA013115.
GeneID693073.
KEGGbmor:693073.

Organism-specific databases

CTD693073.

Phylogenomic databases

OMAIDEMERW.
OrthoDBEOG7XPZ54.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERPTHR11511. PTHR11511. 1 hit.
PfamPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSPR00187. HAEMOCYANIN.
SUPFAMSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRP2_BOMMO
AccessionPrimary (citable) accession number: Q27452
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1999
Last modified: February 19, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families